Stu2p binds tubulin and undergoes an open-to-closed conformational change. - Wikidata - awgldk - TriplyDB

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

http://www.wikidata.org/entity/Q36117307

about

Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1 Structural analysis of Bub3 interactions in the mitotic spindle checkpoint Lessons from in vitro reconstitution analyses of plant microtubule-associated proteins The fission yeast XMAP215 homolog Dis1p is involved in microtubule bundle organization Alp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism.A TOG: -tubulin Complex Structure Reveals Conformation-Based Mechanisms for a Microtubule Polymerase The XMAP215 family drives microtubule polymerization using a structurally diverse TOG array A tethered delivery mechanism explains the catalytic action of a microtubule polymerase Roles for the conserved spc105p/kre28p complex in kinetochore-microtubule binding and the spindle assembly checkpoint.Regulation of microtubule dynamics by Bim1 and Bik1, the budding yeast members of the EB1 and CLIP-170 families of plus-end tracking proteins.Discrete states of a protein interaction network govern interphase and mitotic microtubule dynamics Aspergillus nidulans Dis1/XMAP215 protein AlpA localizes to spindle pole bodies and microtubule plus ends and contributes to growth directionality.XMAP215 is a processive microtubule polymerase.Structural mutants of the spindle pole body cause distinct alteration of cytoplasmic microtubules and nuclear dynamics in multinucleated hyphae.Fission yeast Alp14 is a dose-dependent plus end-tracking microtubule polymerase One-step purification of assembly-competent tubulin from diverse eukaryotic sources.A fluorescent reporter for mapping cellular protein-protein interactions in time and space.The structured core of human β tubulin confers isotype-specific polymerization properties.Detection of alpha-rod protein repeats using a neural network and application to huntingtin.A TOGL domain specifically targets yeast CLASP to kinetochores to stabilize kinetochore microtubules.Stu2, the budding yeast XMAP215/Dis1 homolog, promotes assembly of yeast microtubules by increasing growth rate and decreasing catastrophe frequency The contribution of αβ-tubulin curvature to microtubule dynamics.XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region.CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule.The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly.Drosophila melanogaster mini spindles TOG3 utilizes unique structural elements to promote domain stability and maintain a TOG1- and TOG2-like tubulin-binding surface The cyclin-dependent kinase Cdc28p regulates multiple aspects of Kar9p function in yeast.Katanin Severing and Binding Microtubules Are Inhibited by Tubulin Carboxy Tails Mutations in Human Tubulin Proximal to the Kinesin-Binding Site Alter Dynamic Instability at Microtubule Plus- and Minus-Ends.XMAP215: a tip tracker that really moves.The composition, functions, and regulation of the budding yeast kinetochore Centriole inheritance Gated entry into the ciliary compartment.Regulation of microtubule dynamics by TOG-domain proteins XMAP215/Dis1 and CLASP.Kinetochores generate microtubules with distal plus ends: their roles and limited lifetime in mitosis An unconventional interaction between Dis1/TOG and Mal3/EB1 in fission yeast promotes the fidelity of chromosome segregation.Kinetochore-dependent microtubule rescue ensures their efficient and sustained interactions in early mitosis.Spc24 and Stu2 promote spindle integrity when DNA replication is stalled.A TOG Protein Confers Tension Sensitivity to Kinetochore-Microtubule Attachments.Assembling the protein architecture of the budding yeast kinetochore-microtubule attachment using FRET.

P2860

Q24294735-C079C89F-9832-4919-992A-8A881CE323E2 Q24672093-A254C883-BD65-4CC7-9E6F-610243ED8F61 Q27027026-22F4858A-F720-40C9-AD01-3BE0D0DD1E3F Q27316044-9EDE1DFA-3A40-4417-8049-6A0D1170FFF3 Q27350195-57299E79-D8D4-4E59-895B-1EA51A53F712 Q27671583-17EAB135-DF16-4B1A-B279-69DEB996FA26 Q27684463-548DF26C-8C70-40E7-8D02-4EAC4BAB0CE0 Q27684949-4AE33AA5-385A-4F46-ADAA-CCCD58B9A951 Q27930839-D70E7649-ED2E-464E-8E16-D01B0449B2B2 Q27933184-8F69A825-1E73-472F-824A-1806371BBC07 Q28469115-0CC51B0D-3B21-41A0-B452-BAA1D0CB4BD9 Q30479105-A1299751-5462-46BA-9CA7-FC5F443E0666 Q30481699-6EC41AD3-BE2E-4A31-BDC6-352DED1467C8 Q30493373-DFCD4185-7FCF-46E2-B688-7DD30E896EFF Q30523757-2012C58A-FE5B-453A-881E-FD3FABD6695C Q30528300-A7F99E01-E8E3-449C-A865-7E01B979EE1E Q30538538-70064E1E-8A7E-497C-BF41-CD13AE73912C Q30761012-743716CA-C690-4693-AC06-FC44AC69C415 Q33417634-250722D1-2074-432A-8A03-740AD609CD6E Q33663181-CD583A30-C87A-42F0-A32D-5A4D1FD7097E Q34317259-D17F8119-5EA7-462B-A6EA-4C31EBB70046 Q34483807-E61271E9-5972-4AEC-8C4F-02AD93726EF6 Q34582737-7AD3D32F-4CA7-4EE5-9FE6-D4DDD9587588 Q34622487-ADE2B30A-1C99-4C06-84EF-37C2B2571776 Q35310949-070AA796-1231-4F93-9D20-C34D44F1401B Q35451024-DD92EF40-0257-4412-8174-624B6FEE6FAA Q35723761-9AD76D5D-D477-42FB-91AD-3179CD353516 Q36426507-E27DD7B3-72F5-457D-801F-C4B06155CFD1 Q36800259-C2A4CCA9-B5EB-45A2-B0BB-E5056F2265F3 Q37055556-3032B3F8-E2C8-47C7-A080-CEA4A9823583 Q37063126-257A8C8B-B231-4DA6-87A8-5D2FD292D86D Q37080414-39D9079A-A708-4AFC-9868-527415490116 Q37123963-61F8638C-32E8-4EE6-8859-8BBA3D5F6553 Q37904130-170A68FB-DF9B-4862-B673-E8333210F3D1 Q39277128-186B2E59-2D78-47A7-8576-2A116167CD7F Q40350017-D98A3A44-C26E-4C97-8E09-FAF5A5531D74 Q41050003-7BE60924-203C-48A0-B615-454A28F836D5 Q42414556-39D070D9-56BF-4100-A6CD-B5C650AFC477 Q42741776-7C2E18D2-C7D6-4654-A3FF-307EEB1AA526 Q42928082-C302C290-A701-46D3-85E9-BD053174A496

P2860

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

http://www.wikidata.org/entity/Q36117307

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

2006年论文

@zh

2006年论文

@zh-cn

name

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

@ast

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

@en

type

label

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

@ast

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

@en

prefLabel

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

@ast

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

@en

P1433

Q36117307-8A4151AE-F49F-44D6-ABEC-0A799AF4250A

P1476

Q36117307-CA5AAA21-89D7-4154-A846-F5645FE49FE5

P2093

Q36117307-5906DF57-5944-4C88-8A6B-912A492A7A5B

Q36117307-636929A7-4A7A-4E01-B4A2-F6C216193146

Q36117307-74D93DA8-E777-4B57-832B-79FC27EF57C4

Q36117307-FA2E31AF-041A-4FC9-9494-032F9D483B0D

P2860

Q36117307-0648C3B2-B129-4C73-98C2-95127494B2A2

Q36117307-07E7130F-ED92-407F-98FB-D595214E6C00

Q36117307-0DBB6EBF-245F-4B87-BB10-20493BF26B71

Q36117307-0F0D82D1-2F7D-4000-9F8B-6D06662080C9

Q36117307-2B00EB9E-E435-4E27-8468-7E413844E015

Q36117307-2D3F7FC5-EBC1-4313-9D6C-3163EFFF710C

Q36117307-353B6774-83FF-4D5B-B055-9699FFF719E1

Q36117307-3653AAE2-6E15-48F7-84B6-F4FE13F74E58

Q36117307-423E6F04-266F-430C-BB5A-9BC4E50016B9

Q36117307-46C04543-5C03-4E73-94E4-5654C0DBF92F

P304

Q36117307-3950EA98-53C1-41B6-A7AB-5FE7E0761FDF

P31

Q36117307-11E61C57-DB10-4B32-8740-C964501EE0AD

P356

Q36117307-9298966B-16B0-437C-8D74-76222A816752

P407

Q36117307-9B110789-7BD3-42C3-80D7-2C110E2C0D3B

P433

Q36117307-70DCDF67-86CE-449E-BC2D-DD8E79F14FB4

P478

Q36117307-81029803-F42F-4207-BE2B-BCBCCF197E3E

P577

Q36117307-193F9572-B0F4-46A0-8E51-CAA8953B7ADE

P5875

Q36117307-9587FCBC-4A51-421A-ACCE-F09A97D38076

P698

Q36117307-9771DE1B-1F68-49AD-8CA5-F0C89FA54089

P932

Q36117307-38A5CA50-8317-4D22-9506-BB1B1D51C1A2

P356

P1433

Journal of Cell Biology

P1476

Stu2p binds tubulin and undergoes an open-to-closed conformational change.

@en

P2093

Anthony Hyman

http://www.w3.org/2001/XMLSchema#string

Jawdat Al-Bassam

http://www.w3.org/2001/XMLSchema#string

Mark van Breugel

http://www.w3.org/2001/XMLSchema#string

Stephen C Harrison

http://www.w3.org/2001/XMLSchema#string

P2860

TOGp, the human homolog of XMAP215/Dis1, is required for centrosome integrity, spindle pole organization, and bipolar spindle assembly

Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis

The ch-TOG/XMAP215 protein is essential for spindle pole organization in human somatic cells

Time-lapse microscopy reveals unique roles for kinesins during anaphase in budding yeast.

Molecular analysis of kinetochore-microtubule attachment in budding yeast.

Control of microtubule dynamics by Stu2p is essential for spindle orientation and metaphase chromosome alignment in yeast

Yeast Cdk1 translocates to the plus end of cytoplasmic microtubules to regulate bud cortex interactions.

The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast.

Hierarchical assembly of the budding yeast kinetochore from multiple subcomplexes

CLIP-170 highlights growing microtubule ends in vivo

P304

1009-1022

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1083/JCB.200511010

http://www.w3.org/2001/XMLSchema#string

P407

P433

7

http://www.w3.org/2001/XMLSchema#string

P478

172

http://www.w3.org/2001/XMLSchema#string

P577

2006-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

7210811

http://www.w3.org/2001/XMLSchema#string

P698

16567500

http://www.w3.org/2001/XMLSchema#string

P932

2063759

http://www.w3.org/2001/XMLSchema#string